A kinetic model for binding multifunctional ligand to a surface with a dense homogeneous array of sites was developed and applied to the analysis of the phage inhibition assay, which exploits the loss of bacteriolytic capacity that occurs as a consequence of the phage antibody interaction. For immunoglobulin G. the interaction is a two step process; a bimolecular reaction followed by intramolecular bonding. It was possible to estimate the forward rate constant for the second step (a new number) from availabe data. Some in vitro and in vivo implications of miltisite attachment have been developed as part of a broader collaborative effort with Dr. Henry Metzger, NIMADD, in which factors contributing to observed rate constants were analyzed. The hemolytic plaque assay, which is used world-wide for detecting and enumerating antibody secreting cells, was further analyzed in the presence of an electric field. Immunologists have not attempted electrophoresis experiments which use lymphocytes as an antibody source, but the analysis suggests they are feasible and should be of considerable importance.